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phosphoribosyl pyrophosphate [PRPP] synthetase; ribosephosphate pyrophosphokinase

Function: - catalyzes synthesis of phosphoribosylpyrophosphate (PRPP), essential for nucleotide synthesis - activated by Mg+2 & inorganic phosphate - metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1 ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate Cofactor: Mg+2 Structure: - homodimer - the active form is probably an hexamer composed of 3 homodimers (putative) - belongs to the ribose-phosphate pyrophosphokinase family Pathology: - PRPP synthetase deficiency - PRPP synthetase overactivity leads to hyperuricemia [4] Laboratory: - phophoribosylpyrophosphate synthetase in fibroblasts - phophoribosylpyrophosphate synthetase in erythrocytes

Specific

ribose-phosphate pyrophosphokinase 1; PPribP; phosphoribosyl pyrophosphate synthase 1; PRS-1 (PRPS1) ribose-phosphate pyrophosphokinase 2; PPribP; phosphoribosyl pyrophosphate synthase II; PRS-II (PRPS2) ribose-phosphate pyrophosphokinase 3; phosphoribosyl pyrophosphate synthase 1-like 1; PRPS1-like 1; phosphoribosyl pyrophosphate synthase 3; PRS-3 (PRPS1L1, PRPS3, PRPSL)

General

kinase or ATP-phosphotransferase

Properties

MOTIF: kinase domain MOTIF: ATP-binding site NAME: ATP-binding site binding site FOR-BINDING-OF: H2PO4- Mg+2-binding site

Database Correlations

ENZYME 2.7.6.1

References

  1. UniProt :accession P60891
  2. UniProt :accession P11908
  3. UniProt :accession P21108
  4. Medical Knowledge Self Assessment Program (MKSAP) 17, American College of Physicians, Philadelphia 2015